Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Election/Restrictions
Applicant’s election without traverse of Group I claims 1-82 and 89-91 in the reply filed on 2/20/26 is acknowledged.
Claims 23, 25-26 and 83-88 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention and species, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 2/20/26.
Claim Objections
Claim 2 and 89-91 objected to because of the following informalities:
In claim 2, line 1 please insert “of’ after “cell”.
Claims 89-91 are objected to as being dependent on a non-elected invention. The claims should be amended to incorporate the limitation of claim 88 into claims 89 and 90.
Appropriate correction is required.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claim 66 is dependent on a cancelled claims. There is insufficient antecedent basis for this limitation in the claim.
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claim 12 is rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends.
In claim 12, the fusion protein of claim 1 already comprises the anchoring domain of the GPI anchored protein. Thus, claim 12 does not further limit claim 1. Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claim(s) 1-22, 24, 27, 28, 31-32, 34-55, 67-82 and 89-91 is/are rejected under 35 U.S.C. 103 as being unpatentable over Mahadevan et al. WO 2021007565 01-14-2021 in view of Teymennet-Ramirez et al. Frontiers in Bioengineering and Biotechnology, volume 9, Article 794742, January 10th 2022, 10 pages, Su et al. Biotechnol Lett (2010) 32:1131-1136, Kondo et al. WO2016/017736 and Nonaka et al, US 20170211063 2017-07-27 as evidenced by Uniprot Accession N1PAC8 (6/26/2013)/Appendix A and as evidenced by Mahadevan et al. US20210007384 1-14-2021 (‘Mahadevan ‘384”)and as evidenced by Uniprot Accession A0A096ZM56 07-Jan-2015.
Claim 1: Mahadevan et al disclose an engineered eukaryotic cell such as a yeast cell that expresses a catalytic domain of an enzyme that has activity that removes mannose residues from N-acetyl glucosamine linkage and the eukaryotic cell such as a yeast cell also secretes a recombinant ovomucoid protein. See paragraph 34, 35 and 45.
Mahadevan et al disclose the concept of expressing an enzyme in the microbial host having an activity to remove a glycan by cleaving within a chitobiose core of high mannose and hybrid oligosaccharides on an N-linked glycoprotein and the enzyme comprises EndoH, an OCHl-EndoH fusion or an active fragment of EndoH. See paragraph 35.
Mahadevan et al FIG. IB illustrates a comparison in the glycosylation pattern of native ovomucoid and a recombinant ovomucoid produced in P. pastoris and according to the present disclosure. Shown is a lack of the complex branched glycosylation (including a lack of mannose residues) on the recombinant ovomucoid when produced in a strain of P. pastoris comprising endoglycosidases. See paragraph 55.
Mahadevan et al does not disclose that the engineered yeast expresses and displays the endoH on its surface wherein the endoH comprising its catalytic domain is fused to an anchoring domain of GPI anchored protein and wherein the anchoring domain comprises at least about 200 amino acids and at least about 30% of the residues in the anchoring domain are serines or threonines.
Claim 1 and 68: Mahadevan et al does not disclose a method for expressing a surface-displayed fusion protein comprising a catalytic domain of an enzyme and an anchoring domain of glycosylphosphatidylinositol (GPI)-anchored protein, the method comprising obtaining the engineered eukaryotic cell of claim 1 and culturing the engineered eukaryotic cell under conditions that promote expression of the fusion protein.
Teymennet-Ramirez et al disclose that yeast surface display (YSD) has been extensively used due to several advantages over other, similar systems, which includes: 1) various yeast strains; 2) yeast cells are able to perform eukaryotic post-translational modifications, 3) the ease of cell culture and genetic modification allows the proper folding and secretion of large and complex protein scaffolds. Teymennet-Ramirez et al disclose that when soluble proteins or peptides are linked to the cell surface, they gain biotechnological advantages not met by the soluble state, e.g. ease of recovery, control of the spatial protein orientation, concerted protein interactions with co-displayed proteins to mimic supramolecular complexes and easy cell sorting formats. In addition, Teymennet-Ramirez et al disclose that biochemical and catalytic properties can be improved by immobilizing a protein on the yeast cell surface and that proteins displayed on the surface of yeast cells may show enhanced stability against changes in temperature, pH, organic solvents, and proteases and that YSD can be used for biocatalysis. Teymennet-Ramirez et al discloses several anchor proteins including Sed1 that have been used to display proteins on the Yeast cell surface. See abstract and p. 2 first column and table 1 p. 3.
Su et al disclose surface display of an enzyme in P. pastoris using Sed1 as an anchor protein. Su et al disclose that one promising application is based on the development of novel reaction processes using cells that display enzymes on their surface using anchor proteins such as Sed1,Flo1, alpha-agglutinin and Cwp2. The Sed1 anchor protein is fused to the enzyme and expressed under the control of alcohol oxidase 1 promoter (pAOX1) and the amount of enzyme displayed on surface of P. pastoris was higher than that of free enzyme. See whole reference.
Kondo et al is related to the yeast surface display technology disclosing enzymes, GPI anchors, expression constructs for cell surface display and secretor production including types of promoters, terminators, signal peptide etc.
Sed1 anchoring domain comprises at least about 225 amino acids, at least about 250 amino acids, at least about 275 amino acids, at least about 300 amino acids, at least about 325 amino acids, at least about 350 amino acids, at least about 375 amino acids as evidenced by Uniprot Accession N1PAC8 (6/26/2013).
It would have been prima facie obvious to a person of ordinary skill in the art as of the effective filing date of the instant invention to have modified the yeast cell of Mahadevan et al by making a fusion protein comprising a catalytic domain of the enzyme and an anchoring domain of a GPI anchored protein e.g. Sed1 and engineering the yeast cell to surface display the fusion protein and culturing the resulting engineered eukaryotic cell under conditions that promote expression of the fusion protein as taught by Teymennet-Ramirez et al and Su et al and Kondo et al thus, resulting in the instant invention with a reasonable expectation of success.
The motivation to do so is that Teymennet-Ramirez et al disclose that yeast surface display (YSD) has been extensively used due to several advantages over other, similar systems, where the advantages include the fact that yeast cells are able to perform eukaryotic post-translational modifications and the ease of cell culture and genetic modification allows the proper folding and secretion of large and complex protein scaffolds. Teymennet-Ramirez et al disclose that when soluble proteins or peptides are linked to the cell surface, they gain biotechnological advantages not met by the soluble state, e.g. ease of recovery, control of the spatial protein orientation, concerted protein interactions with co-displayed proteins to mimic supramolecular complexes and easy cell sorting formats. In addition, Teymennet-Ramirez et al disclose that biochemical and catalytic properties can be improved by immobilizing a protein on the yeast cell surface and that proteins displayed on the surface of yeast cells may show enhanced stability against changes in temperature, pH, organic solvents, and proteases and that YSD can be used for biocatalysis. Teymennet-Ramirez et al discloses several anchor proteins including Sed1 that have been used to display proteins on the Yeast cell surface. See abstract and p. 2 first column and table 1 p. 3.
Su et al disclose that surface display of an enzyme in P. pastoris using Sed1 as an anchor protein. Su et al disclose that one promising application is based on the development of novel reaction processes using cells that display enzymes on their surface using anchor proteins such as Sed1,Flo1, alpha-agglutinin and Cwp2 and that in the Sed1 anchor protein is fused to the enzyme and expressed under the control of alcohol oxidase 1 promoter (pAOX1) and the amount of enzyme displayed on surface of P. pastoris was higher than that of free enzyme.
Kondo et al is related to the yeast surface display technology disclosing enzymes, GPI anchors, expression constructs for cell surface display and secretor production including types of promoters, terminators, signal peptide etc. See entirety of Kondo et al.
The teachings of the combination of references that further render the following claims prima facie obvious to a person of ordinary skill in the art as of the effective filing date are set forth below
Claim 3: As evidenced by Uniprot Accession N1PAC8 (6/26/2013) at least about 35% of the residues in the anchoring domain of Sed1 are serines or threonines.
Claim 4: The serines or threonines in the anchoring domain are capable of being O-mannosylated.
Claims 5, 6, : Sed1 anchoring domain comprises at least about 325 amino acids as evidenced by Uniprot Accession N1PAC8, therefore the fusion protein having an anchoring domain comprising at least about 325 amino acids necessarily provides greater enzymatic activity relative to a fusion protein having an anchoring domain comprising less than about 250 or less than about 300 amino acids.
Claim 7: Fusion protein comprises the anchoring domain of the GPI anchored Sed 1 protein.
Claim 8: Teymennet-Ramirez et al disclose the strategy of using a GPI anchored protein without its native signal peptide. See table 1 and under signal peptide sequence on p. 4.
Claim 9-10: The Sed1 protein (GPI anchored protein) is naturally expressed from S. cerevisiae and is not native to the engineered eukaryotic cell such as Pichia pastoris.
Claim 11: The GPI anchored protein is Sed1.
Claim 12-13: Sed1 comprises an amino acid sequence that is 100% identical to SEQ ID NO: 13 and comprises SEQ IDNO: 13. See alignment in Appendix A.
Claim 14-16: Mahadevan et al disclose the engineered eukaryotic cell o is a yeast cell such as Pichia species such as Pichia pastoris. See paragraph 34, 55
Claim 17: The engineered eukaryotic cell of claim 1, wherein the engineered eukaryotic cell comprises an extrachromosomal modification that expresses the fusion protein e.g. transformation of the yeast cell. See Mahadevan et al disclose transformation of the Pichia pastoris with vectors encoding the endoH enzyme as well as a vector encoding the ovomucoid. See example 1. Similarly, Su et al disclose transformation of P. pastoris with vectors comprising Sed1-enzyme fusion protein on the surface of the yeast cells. See figure 1 of Su et al.
Claim 18: the Sed1 protein in the fusion protein comprises a portion of the enzyme in addition to its catalytic domain. See appendix A.
Claim 19: the Sed1 protein in the fusion protein comprises substantially the entire amino acid sequence of the enzyme.
Claim 20: The Sed1 enzyme catalyzes a post-translational modification of the ovomucoid protein secreted by the engineered eukaryotic cell.
Claim 21: The catalyzed post- translational modification comprises deglycosylation. See paragraph 89.
Claim 22: Mahadevan et al disclose the enzyme catalyzing a post-translational modification is endoglycosidase H (endoH).
Claim 23: The endoglycosidase H (endoH) is a glycosidase.
Claim 24: The endoglycosidase H (endoH) is a
is a mannosidase that removes mannose residues from N-acetyl glucosamine linkage; separating the rOVD protein from the host cell. See paragraph 45, 89 and 222.
Claim 27-28: the endoH disclosed by Mahadevan et al comprises an amino acid sequence that is 100% identical to SEQ ID NO: 19 as evidenced by Mahadevan ‘384 disclosing the amino acid sequence of EndoH which is 100% identical to SEQ ID NO: 19. See Appendix B.
Claim 31: In the fusion protein, the catalytic domain is N-terminal to the anchoring domain because the catalytic domain of the enzyme is surface displayed while the anchoring domain of the Sed 1 domain anchors to the cell wall of the eukaryotic cell.
Claim 32: Teymennet Ramirez et al disclose that linkers improves the display efficiencies and the activity of the protein of interest (POI). See p. 5 under linkers or spacers.
Claim 33:
Claim 34: Teymennet-Ramirez et al disclose that native signal peptides of Sed1 can be used -an anchor contains 2 main parts: 1) a signal peptide sequence (SS), involved in protein transport through the protein secretion pathway and 2) anchor to which the protein of interest is fused. See p. 4 under signal peptide sequence.
Teymennet-Ramirez et al disclose that alpha-factor secretion signal can be used for GPI anchored enzyme – see table 1 “secretory pathway modification”. As evidenced by Uniprot Accession A0A096ZM56 alpha factor signal peptide consists of SEQ ID NO: 66. See alignment and sequence annotation.
Claim 35, 37, 39, 41, 43, 44: The engineered eukaryotic cell necessarily will comprises two or more, three or more, or four fusion proteins comprising the same enzyme type in the cell wall.
Claims 35, 36, 38, 40, 42,44: Teymennet-Ramirez et al disclose that and engineered eukaryotic cell of for surface display can display multiple enzymes for co-display wherein the two or more fusion proteins comprise different enzyme types. Thus, co-displaying the enzymes for deglycosylating ovomucoid in paragraph 22 Mahadevan such as endoglucanases (such as EndoH), endoglycosidases, mannosidases (such as alpha- 1,2 mannosidase), PNGase F, O-Glycosidase, OCH1, Neuraminidase, b,1-4 Galactosidase, b-N-acetylglucosaminidases, etc.), deacetylated (e.g., protein deacetylase, histone deacetylase, sirtuin), or dephosphorylated (e.g., acid phosphatase, lambda protein phosphatase, calf intestinal phosphatase, alkaline phosphatase) in different fusions with the different anchor proteins used for surface display such as Sed1, PIR, Aga1, Flo1 would have been prima facie obvious to a person of ordinary skill in the art as of the effective filing date of the instant invention. See Teymennet-Ramirez et al figure 1 p. 4 and p. 5 under multi-enzyme expression and Mahadevan et al paragraphs 220-2221 disclosing that one or more enzymes can be used for modifying the glycosylation of the recombinant ovomucoid protein.
Claim 45:Mahadevan disclose the engineered eukaryotic cell comprises a mutation (deletion) in its AOX1 gene. See paragraph 263.
Claim 46: Mahadevan et al disclose that the engineered eukaryotic cell comprises a genomic modification (deletion of AOX1) that overexpresses a secreted recombinant ovomucoid protein and/or transformation with vectors (extrachromosomal modification) that result in overexpression of secreted recombinant ovomucoid. See portions cited above and example 1.
Claim 47-49: the secreted recombinant protein is an animal protein,
wherein the animal protein is an egg protein such as ovomucoid. See paragraph 89 and 218-222.
Claim 50: Mahadevan et al disclose that the engineered eukaryotic cell comprises a genomic modification and/or the extrachromosomal modification that overexpresses the secreted recombinant protein comprises an inducible promoter. See paragraph 223 and 229.
Claim 51: Mahadevan et al disclose the inducible promoter is an AOX1, FLD1, DAS1, HAC1, GBP2, PEX8 promoter. See paragraph 229. Nonaka et al also disclose that for high level secretory production of proteins in yeast, in addition to the AOX1 and AOX2 gene promoters involved in methanol metabolism, the PMP20 promoter also associated with methanol metabolism are regulated by methanol and are strong promoters generally used to achieve secretory production of various target proteins. See paragraph 7.
Claim 52: Mahadevan et al disclose the genomic modification and/or the extrachromosomal modification that overexpresses a secreted recombinant protein comprises an AOX1 or MOX terminator. See paragraph 232. Furthermore, Kondo et al disclose that the polynucleotide containing the secretion cassette or the surface display cassette can further contain a terminator such as TDH3. See under Terminator DNA.
Claim 53: Mahadevan et al discloses that the secreted ovomucoid comprises alpha mating factor signal sequence fused to the ovomucoid. See paragraph 212, 234, 253-255. Mahadevan ‘384 disclose the sequence of alpha mating factor secretory signal fused to ovomucoid protein wherein the alpha mating factor is 100% identical to SEQ ID NO: 299. See Appendix C.
Claim 54: Mahadevan et al disclose the genomic modification and/or the extrachromosomal modification that overexpresses a secreted recombinant protein comprises codons that are optimized for the species of the engineered eukaryotic cell. See paragraph 231.
Claim 55: Mahadevan et al disclose the secreted recombinant protein is designed to be secreted from the cell and/or is capable of being secreted from the cell. See paragraph 212.
Claim 66: The modified eukaryotic cell further genomic modification i.e. signal peptide sequence that promotes trafficking of the surface-displayed fusion protein through the secretory pathway as taught by Teymennet-Ramirez et a. p. 4 under signal peptide sequence.
Claim 67: The engineered eukaryotic cell comprises encodes one or more additional fusion proteins comprising a catalytic domain of an enzyme and an adhesion or anchoring domain from a cell surface protein in the case multi-enzyme expression and any of the anchoring domains such as Sed1, Flo1, and PIR with the adhesion or anchoring domain having the ability to capture exopolysaccharides and retain the additional fusion protein at the extracellular surface. See table 1 of Teymennet-Ramirez et al.
Claim 69-71: as set forth above, the engineered eukaryotic cell comprises a genomic modification and/or an extrachromosomal modification that overexpresses a secreted recombinant protein comprises an inducible promoter. Furthermore, Mahadevan et al, Teymennet-Ramirez et al and Su disclose several inducible promoters that can be employed in the method of culturing the engineered eukaryotic cell under conditions that promote expression of the fusion protein by contacting the engineered eukaryotic with an agent that activates the inducible promoter. The promoters are listed above as disclosed by Mahadevan et al, Su et al disclose use of AOX1 inducible promoter and Teymennet-Ramirez et al disclose other inducible promotors ins table 1 such as SEQ1, AOX1 etc. Mahadevan et al disclose DAS1, PEX11, AOX1 is inducible by methanol, for example. See paragraph 229, 262-264.
Nonaka et al also disclose that for high level secretory production of proteins in yeast, in addition to the AOX1 and AOX2 gene promoters involved in methanol metabolism, the PMP20 promoter also associated with methanol metabolism are regulated by methanol and are strong promoters generally used to achieve secretory production of various target proteins. See paragraph 7.
Claim 72: Mahadevan et al disclose the recombinant ovomucoid is designed to be secreted from the cell and/or is capable of being secreted from the cell.
Claim 73: the combination of Mahadevan, Teymennet-Ramirez and Sue results in a population of engineered eukaryotic cells.
Claim 74: the combination of Mahadevan, Teymennet-Ramirez and Sue disclose a bioreactor comprising the population of engineered eukaryotic cells. See paragraph 257.
Claim 75: the combination of Mahadevan, Teymennet-Ramirez and Sue disclose a composition comprising the engineered eukaryotic cell and the secreted recombinant protein e.g. in the bioreactor.
Claim 76-78: the secreted recombinant protein is an animal protein is ovomucoid.
Claim 79-82: The combination of Mahadevan, Teymennet-Ramirez and Sue et al disclose the composition comprising an engineered eukaryotic cell, a secreted recombinant protein that has been deglycosylated, and one or more oligosaccharides cleaved from the secreted recombinant protein ovomucoid by the surface displayed enzyme e.g. in the bioreactor.
Claims 89-91: the combination of Mahadevan, Teymennet-Ramirez and Sue et al disclose a polynucleotide, vectors and host cells encoding the surface-displayed fusion protein comprising a catalytic domain of the enzyme and an anchoring domain of the GPI anchored protein e.g. Sed1 that comprises at least about 200 amino acids and/or at least about 30% of the residues in the anchoring domain are serines or threonines.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 1-15, 17-22, 27-35, 37, 39, 41, 43, 44, 45-49, 55, 67, 68, 72, 73, 75-82 and 89-91 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-2,9 , 10, 13, 22-23, 26, 28, 29, 31, 34, 35-41, 43-46,48, 50, 51, 58-61, 64-65, 68, and 88 of copending Application No. 18,346,022 (‘022). Although the claims at issue are not identical, they are not patentably distinct from each other because the ‘022 claims disclose
An engineered eukaryotic cell that expresses a surface-displayed fusion protein comprising a catalytic domain of an enzyme and an anchoring domain of a glycosylphosphatidylinositol (GPI)-anchored protein, wherein the anchoring domain comprises at least about 200 amino acids, and at least about 30% of the residues in the anchoring domain are serines or threonines.
The engineered eukaryotic cell comprises a fusion protein comprising SEQ ID NO: 26 (see SEQ ID NO: 10 of the ‘022 claims) which comprises Sed1 anchor, linker (corresponding to SEQ ID NO: 31) and endoglycosidase H (endoH).
The ‘022 claims disclose the anchoring domain is N-terminal to the catalytic domain in the fusion protein or C-terminal to the catalytic domain in the fusion protein.
The ‘022 claims disclose the anchoring domain can be non-native and the fusion protein comprises an amino acid sequence that is at least 95% identical to is capable of binding an exopolysaccharide present on the surface of the cell and thereby attaching the fusion protein to the extracellular surface of the cell for surface display.
The eukaryotic cell comprises a mutation in its AOX1 gene and it is Pichia species and overexpresses ovomucoid and the nucleic acid sequence encoding the fusion protein can be extrachromosomal. The cell further encodes a fusion protein comprising a catalytic domain of an enzyme and an adhesion domain that is capable of binding an exopolysaccharide present on the surface of the cell and thereby attaches the fusion protein to the extracellular surface of the cell for surface display and disclose Sedlp, Flo5-2, or Flo11 anchoring domains.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 1-22, 27-35, 37, 39, 41, 43, 44, 45-49, 50-55, 68, 69-82 and 89-91 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-67 of copending Application No. 18,346,095 (‘095). Although the claims at issue are not identical, they are not patentably distinct from each other because the ‘095 claims disclose
An engineered eukaryotic cell that expresses a surface-displayed fusion protein comprising a catalytic domain of an enzyme and an anchoring domain of a glycosylphosphatidylinositol (GPI)-anchored protein, wherein the anchoring domain comprises at least about 200 amino acids, and at least about 30% of the residues in the anchoring domain are serines or threonines.
The engineered eukaryotic cell comprises a fusion protein comprising SEQ ID NO: 26 (see SEQ ID NO: 10 of the ‘95 claims) which comprises Sed1 anchor, linker (corresponding to SEQ ID NO: 31) and endoglycosidase H (endoH).
The ‘095 claims disclose the anchoring domain is N-terminal to the catalytic domain in the fusion protein or C-terminal to the catalytic domain in the fusion protein.
The ‘095 claims disclose the anchoring domain can be non-native
The eukaryotic cell comprises a mutation in its AOX1 gene and it is Pichia pastoris species and overexpresses ovomucoid and the nucleic acid sequence encoding the fusion protein can be extrachromosomal. The ‘095 claims disclose the nucleic acid encoding the fusion protein comprises an inducible promoter and terminator. The cell further encodes a fusion protein comprising a catalytic domain of an enzyme and an adhesion domain that is capable of binding an exopolysaccharide present on the surface of the cell and thereby attaches the fusion protein to the extracellular surface of the cell for surface display and disclose Sedlp, Flo5-2, or Flo11 anchoring domains.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 1-22, 31-35, 37, 39, 41, 43, 44, 46-49, 50-55, 68, 69-73, 75-82 and 89-91 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-2, 5-6, 9-10, 13, 15-17, 19, 21-22, 25 27, 29-31, 33, 34, 37, 39, 40, 41 and 46 of copending Application No. 18,344,773 (‘773). Although the claims at issue are not identical, they are not patentably distinct from each other because the ‘095 claims disclose
An engineered eukaryotic cell that expresses a surface-displayed fusion protein comprising a catalytic domain of an enzyme and an anchoring domain of a glycosylphosphatidylinositol (GPI)-anchored protein, wherein the anchoring domain comprises at least about 200 amino acids, and at least about 30% of the residues in the anchoring domain are serines or threonines.
The engineered eukaryotic cell comprises a fusion protein comprising SEQ ID NO: 26 (see SEQ ID NO: 332,334 of the ‘773 claims) which comprises Sed1 anchor, linker (corresponding to SEQ ID NO: 31) and endoglycosidase H (endoH).
The ‘773 claims disclose the anchoring domain is N-terminal to the catalytic domain in the fusion protein or C-terminal to the catalytic domain in the fusion protein.
The ‘773 claims disclose the anchoring domain can be non-native
The eukaryotic cell comprises a mutation in its AOX1 gene and it is Pichia pastoris species and overexpresses ovomucoid and the nucleic acid sequence encoding the fusion protein can be extrachromosomal. The ‘773 claims disclose the nucleic acid encoding the fusion protein comprises an inducible promoter and terminator s The cell further encodes a fusion protein comprising a catalytic domain of an enzyme and an adhesion domain that is capable of binding an exopolysaccharide present on the surface of the cell and thereby attaches the fusion protein to the extracellular surface of the cell for surface display and disclose Sedlp anchoring domains.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Status of Claims
Status of Claims
Claims 1-22,24, 27-55, 66-82 and 89-91 are rejected. Claims 23, 25-26 and 83-88 are withdrawn.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to OLUWATOSIN A OGUNBIYI whose telephone number is (571)272-9939. The examiner can normally be reached IFP.
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/OLUWATOSIN A OGUNBIYI/ Primary Examiner, Art Unit 1645